[Physiological importance of the microvilli-bound leucine arylamidase in the final digestion of proteins. III. Exopeptidatic activities of purified microvilli against peptides mixtures in the presence and after the removal of free amino acids].
The exopeptidatic degradation of peptide mixtures by the aminopeptidase of the microvilli is inhibited by the presence of free amino acids. Further degradation occurs after the removal of the free amino acids from the peptide mixture. The amino-acid composition of the remaining residual peptides is a second factor that impedes the complete cleavage of the peptides.
D000596:Amino Acids / Q000494:pharmacology*; D000818:Animals; D002462:Cell Membrane / Q000201:enzymology*; D007413:Intestinal Mucosa / Q000201:enzymology; D007421:Intestine, Small / Q000201:enzymology; D007700:Kinetics; D007931:Leucyl Aminopeptidase / Q000378:metabolism*; D008871:Microvilli / Q000201:enzymology*; D010189:Pancreatic Juice / Q000378:metabolism; D010434:Pepsin A / Q000378:metabolism; D010446:Peptide Fragments; D051381:Rats; D013379:Substrate Specificity
D000596:Amino Acids; D010446:Peptide Fragments; D007931:Leucyl Aminopeptidase; D010434:Pepsin A
Untersuchungen zur physiologischen Bedeutung der bürstensaumgebundenen Leucinarylamidase für die Endverdauung von Proteinen. 3. Mitt. Die exopeptidatische Aktivität gereinigter Bürstensäume gegenüber Peptidgemischen in Anwesenheit und nach Abtrennung freier Aminosäuren.